Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/88033
Title: Insights into Biofilm Dispersal Regulation from the Crystal Structure of the PAS-GGDEF-EAL Region of RbdA from Pseudomonas aeruginosa
Authors: Liu, Chong
Liew, Chong Wai
Wong, Yee Hwa
Tan, Siok Thing
Poh, Wee Han
Manimekalai, Malathy S. S.
Rajan, Sreekanth
Xin, Lingyi
Liang, Zhao-Xun
Grüber, Gerhard
Rice, Scott A.
Lescar, Julien
Keywords: Cyclic Di-GMP
PAS Domain
Issue Date: 2018
Source: Liu, C., Liew, C. W., Wong, Y. H., Tan, S. T., Poh, W. H., Manimekalai, M. S. S., et al. (2018). Insights into Biofilm Dispersal Regulation from the Crystal Structure of the PAS-GGDEF-EAL Region of RbdA from Pseudomonas aeruginosa. Journal of Bacteriology, 200(3), e00515-17-.
Series/Report no.: Journal of Bacteriology
Abstract: RbdA is a positive regulator of biofilm dispersal of Pseudomonas aeruginosa. Its cytoplasmic region (cRbdA) comprises an N-terminal Per-ARNT-Sim (PAS) domain followed by a diguanylate cyclase (GGDEF) domain and an EAL domain, whose phosphodiesterase activity is allosterically stimulated by GTP binding to the GGDEF domain. We report crystal structures of cRbdA and of two binary complexes: one with GTP/Mg2+ bound to the GGDEF active site and one with the EAL domain bound to the c-di-GMP substrate. These structures unveil a 2-fold symmetric dimer stabilized by a closely packed N-terminal PAS domain and a noncanonical EAL dimer. The autoinhibitory switch is formed by an α-helix (S-helix) immediately N-terminal to the GGDEF domain that interacts with the EAL dimerization helix (α6-E) of the other EAL monomer and maintains the protein in a locked conformation. We propose that local conformational changes in cRbdA upon GTP binding lead to a structure with the PAS domain and S-helix shifted away from the GGDEF-EAL domains, as suggested by small-angle X-ray scattering (SAXS) experiments. Domain reorientation should be facilitated by the presence of an α-helical lever (H-helix) that tethers the GGDEF and EAL regions, allowing the EAL domain to rearrange into an active dimeric conformation.
URI: https://hdl.handle.net/10356/88033
http://hdl.handle.net/10220/44542
ISSN: 0021-9193
DOI: http://dx.doi.org/10.1128/JB.00515-17
Rights: © 2018 American Society for Microbiology. This paper was published in Journal of Bacteriology and is made available as an electronic reprint (preprint) with permission of American Society for Microbiology. The published version is available at: [http://dx.doi.org/10.1128/JB.00515-17]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
metadata.item.grantfulltext: open
metadata.item.fulltext: With Fulltext
Appears in Collections:IGS Journal Articles
SBS Journal Articles
SCELSE Journal Articles

Google ScholarTM

Check

Altmetric

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.